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Conserved domains on  [gi|58331268|ref|NP_060139|]
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DNA excision repair protein ERCC-6-like isoform a [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12784833)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; such as human DNA excision repair protein ERCC-6-like and DNA repair and recombination protein RAD54-like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
96-328 1.82e-150

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


:

Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 451.83  E-value: 1.82e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYrDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKT 175
Cdd:cd18001    1 LYPHQREGVAWLWSLH-DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLL 255
Cdd:cd18001   80 FHGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331268  256 TGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRR 328
Cdd:cd18001  160 TGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
90-610 1.79e-138

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 437.35  E-value: 1.79e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   90 RELHNQLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTP 169
Cdd:COG0553  236 AGLKATLRPYQLEGAAWLLFLRRLG-LGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  170 GMRVKTFHGPskDERTRNLNRIQQRNgVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPA 249
Cdd:COG0553  315 GLRVLVLDGT--RERAKGANPFEDAD-LVITSYGLLRRDIELLAAVD-----WDLVILDEAQHIKNPATKRAKAVRALKA 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDAtpgekalgfkisENLMAIIKPYFLRRT 329
Cdd:COG0553  387 RHRLALTGTPVENRLEELWSLLDFLNPG-LLGSLKAFRERFARPIEKGDEEAL------------ERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  330 KEDVQKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYRKFVSL--DHIKELLMETR--SPLAELG 405
Cdd:COG0553  454 KEDVLK------------------------DLPEKTEETLYVELTPEQRALYEAVLEYlrRELEGAEGIRRrgLILAALT 509
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  406 VLKKLCDHPRLLSAraccllnlgtfsaqdgnegedspdvdhidqvTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQS 485
Cdd:COG0553  510 RLRQICSHPALLLE-------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  486 RQILNIIERLLKNRHFKTLRIDGTvTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQ 565
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGG-TSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQ 637
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 58331268  566 AVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTG 610
Cdd:COG0553  638 AIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
 
Name Accession Description Interval E-value
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
96-328 1.82e-150

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 451.83  E-value: 1.82e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYrDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKT 175
Cdd:cd18001    1 LYPHQREGVAWLWSLH-DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLL 255
Cdd:cd18001   80 FHGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331268  256 TGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRR 328
Cdd:cd18001  160 TGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
90-610 1.79e-138

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 437.35  E-value: 1.79e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   90 RELHNQLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTP 169
Cdd:COG0553  236 AGLKATLRPYQLEGAAWLLFLRRLG-LGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  170 GMRVKTFHGPskDERTRNLNRIQQRNgVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPA 249
Cdd:COG0553  315 GLRVLVLDGT--RERAKGANPFEDAD-LVITSYGLLRRDIELLAAVD-----WDLVILDEAQHIKNPATKRAKAVRALKA 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDAtpgekalgfkisENLMAIIKPYFLRRT 329
Cdd:COG0553  387 RHRLALTGTPVENRLEELWSLLDFLNPG-LLGSLKAFRERFARPIEKGDEEAL------------ERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  330 KEDVQKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYRKFVSL--DHIKELLMETR--SPLAELG 405
Cdd:COG0553  454 KEDVLK------------------------DLPEKTEETLYVELTPEQRALYEAVLEYlrRELEGAEGIRRrgLILAALT 509
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  406 VLKKLCDHPRLLSAraccllnlgtfsaqdgnegedspdvdhidqvTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQS 485
Cdd:COG0553  510 RLRQICSHPALLLE-------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  486 RQILNIIERLLKNRHFKTLRIDGTvTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQ 565
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGG-TSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQ 637
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 58331268  566 AVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTG 610
Cdd:COG0553  638 AIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
68-607 3.45e-67

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 247.02  E-value: 3.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    68 EELAEQGDDEFTDVCNSGLLLYRE-LHNQLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVN 146
Cdd:PLN03142  141 EEYLKEEEDGLGGSGGTRLLVQPScIKGKMRDYQLAGLNWLIRLYENG-INGILADEMGLGKTLQTISLLGYLHEYRGIT 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   147 --HvLLIMPTNLINTWVKEFIKWTPGMRVKTFHGpSKDERTRNLNRIQQRNG--VIITTYQMLInnwQQLSSFRgqEFVW 222
Cdd:PLN03142  220 gpH-MVVAPKSTLGNWMNEIRRFCPVLRAVKFHG-NPEERAHQREELLVAGKfdVCVTSFEMAI---KEKTALK--RFSW 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   223 DYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKmeyenpitrarEKDA 302
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP-EIFSSAETFD-----------EWFQ 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   303 TPGEKALGfKISENLMAIIKPYFLRRTKEDVQKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYR 382
Cdd:PLN03142  361 ISGENDQQ-EVVQQLHKVLRPFLLRRLKSDVEK------------------------GLPPKKETILKVGMSQMQKQYYK 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   383 KFVSLDhikellMET------RSPLAELGV-LKKLCDHPRLLSAraccllnlgtfsaqdgneGEDSPDVdhidqVTDDTL 455
Cdd:PLN03142  416 ALLQKD------LDVvnaggeRKRLLNIAMqLRKCCNHPYLFQG------------------AEPGPPY-----TTGEHL 466
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   456 MEESGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTvTHLLEREKRINLFqqNKDYS---VF 532
Cdd:PLN03142  467 VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGN-TGGEDRDASIDAF--NKPGSekfVF 543
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331268   533 LLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFK---DSLIRQ 607
Cdd:PLN03142  544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKlalDALVIQ 621
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
99-417 1.21e-66

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 226.80  E-value: 1.21e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     99 HQKEGIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLV--NHVLLIMPTNLINTWVKEFIKWT--PGMRVK 174
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    175 TFHGPSKDERTRNLNRIQQRN-GVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASNRL 253
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADfDVVITTYETLRKHKELLKKVH-----WHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    254 LLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKdatpgekalgfKISENLMAIIKPYFLRRTKEDV 333
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPG-PFGSLSTFRNWFDRPIERGGGK-----------KGVSRLHKLLKPFLLRRTKKDV 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    334 QKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMET------RSPLAELGVL 407
Cdd:pfam00176  224 EK------------------------SLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRL 279
                          330
                   ....*....|
gi 58331268    408 KKLCDHPRLL 417
Cdd:pfam00176  280 RKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
459-585 6.08e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 193.08  E-value: 6.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  459 SGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKDYSVFLLTTQV 538
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSK-ERQKLVDRFNEDPDIRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 58331268  539 GGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLI 585
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
88-273 1.08e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268      88 LYRELHNQLFEHQKEGIAFLYSLYRDGrkggILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPT-NLINTWVKEFIK 166
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDV----ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKK 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     167 WTPGMRVKT---FHGPSKDERTRNLNRiqQRNGVIITTYQMLINNWQQLSSFRGQefvWDYVILDEAHKIKTSSTKS--- 240
Cdd:smart00487   77 LGPSLGLKVvglYGGDSKREQLRKLES--GKTDILVTTPGRLLDLLENDKLSLSN---VDLVILDEAHRLLDGGFGDqle 151
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 58331268     241 AICARAIPASNRLLLTGTP---IQNNLQELWSLFDF 273
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVF 187
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
460-574 1.35e-25

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    460 GKMIFLMDLLKRLRdeGHQTLVFSQSRQILNIiERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKdySVFLLTTQVG 539
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQE-EREEILEDFRKGK--IDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 58331268    540 GVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIG 574
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
491-574 6.27e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 6.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     491 IIERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKdySVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRV 570
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQE-EREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 58331268     571 YRIG 574
Cdd:smart00490   79 GRAG 82
 
Name Accession Description Interval E-value
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
96-328 1.82e-150

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 451.83  E-value: 1.82e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYrDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKT 175
Cdd:cd18001    1 LYPHQREGVAWLWSLH-DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAIPASNRLLL 255
Cdd:cd18001   80 FHGTSKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSADDHDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331268  256 TGTPIQNNLQELWSLFDFACQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRR 328
Cdd:cd18001  160 TGTPIQNNLKELWALFDFACNGSLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
90-610 1.79e-138

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 437.35  E-value: 1.79e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   90 RELHNQLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTP 169
Cdd:COG0553  236 AGLKATLRPYQLEGAAWLLFLRRLG-LGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  170 GMRVKTFHGPskDERTRNLNRIQQRNgVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPA 249
Cdd:COG0553  315 GLRVLVLDGT--RERAKGANPFEDAD-LVITSYGLLRRDIELLAAVD-----WDLVILDEAQHIKNPATKRAKAVRALKA 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDAtpgekalgfkisENLMAIIKPYFLRRT 329
Cdd:COG0553  387 RHRLALTGTPVENRLEELWSLLDFLNPG-LLGSLKAFRERFARPIEKGDEEAL------------ERLRRLLRPFLLRRT 453
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  330 KEDVQKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYRKFVSL--DHIKELLMETR--SPLAELG 405
Cdd:COG0553  454 KEDVLK------------------------DLPEKTEETLYVELTPEQRALYEAVLEYlrRELEGAEGIRRrgLILAALT 509
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  406 VLKKLCDHPRLLSAraccllnlgtfsaqdgnegedspdvdhidqvTDDTLMEESGKMIFLMDLLKRLRDEGHQTLVFSQS 485
Cdd:COG0553  510 RLRQICSHPALLLE-------------------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  486 RQILNIIERLLKNRHFKTLRIDGTvTHLLEREKRINLFQQNKDYSVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQ 565
Cdd:COG0553  559 TDTLDLLEERLEERGIEYAYLHGG-TSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQ 637
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 58331268  566 AVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFKDSLIRQTTG 610
Cdd:COG0553  638 AIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
96-280 3.69e-69

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 229.76  E-value: 3.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYrDGRKGGILADDMGLGKTVQIIAFLSGMFDASL-VNHVLLIMPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd17919    1 LRPYQLEGLNFLLELY-ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKeRGPVLVVCPLSVLENWEREFEKWTPDLRVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASNRLL 254
Cdd:cd17919   80 VYHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFR-----WDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                        170       180
                 ....*....|....*....|....*.
gi 58331268  255 LTGTPIQNNLQELWSLFDFACQGSLL 280
Cdd:cd17919  155 LTGTPLQNNLEELWALLDFLDPPFLL 180
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
92-330 1.69e-68

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 229.37  E-value: 1.69e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   92 LHNQLFEHQKEGIAFLYSLYRDGRkGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGM 171
Cdd:cd18012    1 LKATLRPYQKEGFNWLSFLRHYGL-GGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  172 RVKTFHGPskdERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASN 251
Cdd:cd18012   80 KVLVIHGT---KRKREKLRALEDYDLVITSYGLLRRDIELLKEVK-----FHYLVLDEAQNIKNPQTKTAKAVKALKADH 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331268  252 RLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDAtpgekalgfkiSENLMAIIKPYFLRRTK 330
Cdd:cd18012  152 RLALTGTPIENHLGELWSIFDFLNPG-LLGSYKRFKKRFAKPIEKDGDEEA-----------LEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
68-607 3.45e-67

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 247.02  E-value: 3.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    68 EELAEQGDDEFTDVCNSGLLLYRE-LHNQLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVN 146
Cdd:PLN03142  141 EEYLKEEEDGLGGSGGTRLLVQPScIKGKMRDYQLAGLNWLIRLYENG-INGILADEMGLGKTLQTISLLGYLHEYRGIT 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   147 --HvLLIMPTNLINTWVKEFIKWTPGMRVKTFHGpSKDERTRNLNRIQQRNG--VIITTYQMLInnwQQLSSFRgqEFVW 222
Cdd:PLN03142  220 gpH-MVVAPKSTLGNWMNEIRRFCPVLRAVKFHG-NPEERAHQREELLVAGKfdVCVTSFEMAI---KEKTALK--RFSW 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   223 DYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKmeyenpitrarEKDA 302
Cdd:PLN03142  293 RYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLP-EIFSSAETFD-----------EWFQ 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   303 TPGEKALGfKISENLMAIIKPYFLRRTKEDVQKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYR 382
Cdd:PLN03142  361 ISGENDQQ-EVVQQLHKVLRPFLLRRLKSDVEK------------------------GLPPKKETILKVGMSQMQKQYYK 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   383 KFVSLDhikellMET------RSPLAELGV-LKKLCDHPRLLSAraccllnlgtfsaqdgneGEDSPDVdhidqVTDDTL 455
Cdd:PLN03142  416 ALLQKD------LDVvnaggeRKRLLNIAMqLRKCCNHPYLFQG------------------AEPGPPY-----TTGEHL 466
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   456 MEESGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTvTHLLEREKRINLFqqNKDYS---VF 532
Cdd:PLN03142  467 VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGN-TGGEDRDASIDAF--NKPGSekfVF 543
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331268   533 LLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVEEKIYRRQVFK---DSLIRQ 607
Cdd:PLN03142  544 LLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKlalDALVIQ 621
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
99-417 1.21e-66

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 226.80  E-value: 1.21e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     99 HQKEGIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLV--NHVLLIMPTNLINTWVKEFIKWT--PGMRVK 174
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    175 TFHGPSKDERTRNLNRIQQRN-GVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASNRL 253
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNFLADfDVVITTYETLRKHKELLKKVH-----WHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    254 LLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKdatpgekalgfKISENLMAIIKPYFLRRTKEDV 333
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPG-PFGSLSTFRNWFDRPIERGGGK-----------KGVSRLHKLLKPFLLRRTKKDV 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    334 QKkkssnpearlneknpdvdaicempSLSRKNDLIIWIRLVPLQEEIYRKFVSLDHIKELLMET------RSPLAELGVL 407
Cdd:pfam00176  224 EK------------------------SLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEggreikASLLNILMRL 279
                          330
                   ....*....|
gi 58331268    408 KKLCDHPRLL 417
Cdd:pfam00176  280 RKICNHPGLI 289
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
96-328 5.61e-59

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 202.90  E-value: 5.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGG----ILADDMGLGKTVQIIAFL-----SGMFDASLVNHVLLIMPTNLINTWVKEFIK 166
Cdd:cd18004    1 LRPHQREGVQFLYDCLTGRRGYGgggaILADEMGLGKTLQAIALVwtllkQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  167 WTPGMRVKTFhgpSKDERTRNLNRIQQRNG------VIITTY---QMLINNWQQLSSFrgqefvwDYVILDEAHKIKTSS 237
Cdd:cd18004   81 WLGLRRIKVV---TADGNAKDVKASLDFFSsastypVLIISYetlRRHAEKLSKKISI-------DLLICDEGHRLKNSE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  238 TKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENL 317
Cdd:cd18004  151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPG-ILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQEL 229
                        250
                 ....*....|.
gi 58331268  318 MAIIKPYFLRR 328
Cdd:cd18004  230 SELTSRFILRR 240
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
459-585 6.08e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 193.08  E-value: 6.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  459 SGKMIFLMDLLKRLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKDYSVFLLTTQV 538
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSK-ERQKLVDRFNEDPDIRVFLLSTKA 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 58331268  539 GGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLI 585
Cdd:cd18793   89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
96-328 1.86e-54

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 190.28  E-value: 1.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRkGGILADDMGLGKTVQIIAFLSGMF---------------------DASLVNHVLLIMPT 154
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGR-GGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfkkkppASSAKKPVLIVAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  155 NLINTWVKEFIKWtpG-MRVKTFHGpSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKI 233
Cdd:cd18005   80 SVLYNWKDELDTW--GhFEVGVYHG-SRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSIN-----WSAVIADEAHRI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  234 KTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSlLGTLKTFKMEYENPITRAREKDATPGEKALGFKI 313
Cdd:cd18005  152 KNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGA-LGSRSQFKKHFSEPIKRGQRHTATARELRLGRKR 230
                        250
                 ....*....|....*
gi 58331268  314 SENLMAIIKPYFLRR 328
Cdd:cd18005  231 KQELAVKLSKFFLRR 245
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
96-273 1.59e-53

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 185.61  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDgRKGGILADDMGLGKTVQIIAFLSGM-FDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQ-RVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFH----------GPSKDERTRNLNR-IQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAIC 243
Cdd:cd18000   80 VLHssgsgtgseeKLGSIERKSQLIRkVVGDGGILITTYEGFRKHKDLLLNHN-----WQYVILDEGHKIRNPDAEITLA 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 58331268  244 ARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18000  155 CKQLRTPHRLILSGTPIQNNLKELWSLFDF 184
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
95-330 1.14e-51

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 181.82  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd18009    3 VMRPYQLEGMEWLRMLWENGING-ILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGPsKDERTRNLNRIQQR------NGVIITTYQMLINNWQQLssfrgQEFVWDYVILDEAHKIKTSSTKSAICARAIP 248
Cdd:cd18009   82 LYHGT-KEERERLRKKIMKRegtlqdFPVVVTSYEIAMRDRKAL-----QHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  249 ASNRLLLTGTPIQNNLQELWSLFDFacqgsLLGT----LKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPY 324
Cdd:cd18009  156 SDNRLLLTGTPLQNNLSELWSLLNF-----LLPDvfddLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPF 230

                 ....*.
gi 58331268  325 FLRRTK 330
Cdd:cd18009  231 LLRRLK 236
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
96-328 3.37e-48

DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350757 [Multi-domain]  Cd Length: 232  Bit Score: 171.77  E-value: 3.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGI---AFL--YSLYrdgrkgGILADDMGLGKTVQIIAFLSGMFDASLVNH------VLLIMPTNLINTWVKEF 164
Cdd:cd17999    1 LRPYQQEGInwlAFLnkYNLH------GILCDDMGLGKTLQTLCILASDHHKRANSFnsenlpSLVVCPPTLVGHWVAEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  165 IKWTP--GMRVKTFHGPSKDERTrnLNRIQQRNGVIITTYQMLINNWQQLssfrgQEFVWDYVILDEAHKIKTSSTKSAI 242
Cdd:cd17999   75 KKYFPnaFLKPLAYVGPPQERRR--LREQGEKHNVIVASYDVLRNDIEVL-----TKIEWNYCVLDEGHIIKNSKTKLSK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  243 CARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIK 322
Cdd:cd17999  148 AVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPG-YLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVL 226

                 ....*.
gi 58331268  323 PYFLRR 328
Cdd:cd17999  227 PFLLRR 232
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
99-328 5.37e-46

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 165.40  E-value: 5.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   99 HQKEGIAFLY----SLYRDGRKGGILADDMGLGKTVQIIAFL-----SGMFDAS-LVNHVLLIMPTNLINTWVKEFIKWT 168
Cdd:cd18066    4 HQREGIEFLYecvmGMRVNERFGAILADEMGLGKTLQCISLIwtllrQGPYGGKpVIKRALIVTPGSLVKNWKKEFQKWL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  169 PGMRVKTFhGPSKDERTRNLNRiQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIP 248
Cdd:cd18066   84 GSERIKVF-TVDQDHKVEEFIA-SPLYSVLIISYEMLLRSLDQISKLN-----FDLVICDEGHRLKNTSIKTTTALTSLS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  249 ASNRLLLTGTPIQNNLQELWSLFDFaCQGSLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAIIKPYFLRR 328
Cdd:cd18066  157 CERRIILTGTPIQNDLQEFFALIDF-VNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
93-330 8.18e-45

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 161.72  E-value: 8.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   93 HNQLFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVN--HvLLIMPTNLINTWVKEFIKWTPG 170
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGING-ILADEMGLGKTLQTISLLGYLKHYKNINgpH-LIIVPKSTLDNWMREFKRWCPS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  171 MRVKTFHGpSKDERTRNLNR--IQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIP 248
Cdd:cd17997   79 LRVVVLIG-DKEERADIIRDvlLPGKFDVCITSYEMVIKEKTVLKKFN-----WRYIIIDEAHRIKNEKSKLSQIVRLFN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  249 ASNRLLLTGTPIQNNLQELWSLFDFacqgsLL----GTLKTFKMEYENpitrarEKDATPGEkalgfKISENLMAIIKPY 324
Cdd:cd17997  153 SRNRLLLTGTPLQNNLHELWALLNF-----LLpdvfTSSEDFDEWFNV------NNCDDDNQ-----EVVQRLHKVLRPF 216

                 ....*.
gi 58331268  325 FLRRTK 330
Cdd:cd17997  217 LLRRIK 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
96-309 8.37e-45

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 162.08  E-value: 8.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYS------LYRDGRKGGILADDMGLGKTVQIIAFL-SGMFDASLVNHVLLIMPTNLINTWVKEFIKWT 168
Cdd:cd18007    1 LKPHQVEGVRFLWSnlvgtdVGSDEGGGCILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  169 PGMRV--KTFHGPSK----DERTRNLNRIQQRNGVIITTYQM---LINNWQQLSSFRGQEFVW------DYVILDEAHKI 233
Cdd:cd18007   81 PPDLRplLVLVSLSAskraDARLRKINKWHKEGGVLLIGYELfrnLASNATTDPRLKQEFIAAlldpgpDLLVLDEGHRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58331268  234 KTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFAcQGSLLGTLKTFKMEYENPITRAREKDATPGEKAL 309
Cdd:cd18007  161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA-RPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRL 235
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
96-328 9.16e-45

DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350766 [Multi-domain]  Cd Length: 241  Bit Score: 162.07  E-value: 9.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSlyrdgrKGGILADDMGLGKTVQIIA---------------FLSGMFDASLVNHV---LLIMPTNLI 157
Cdd:cd18008    1 LLPYQKQGLAWMLP------RGGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYLSkttLIVVPLSLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  158 NTWVKEFIK--WTPGMRVKTFHGPSKDERTRNLNRIqqrnGVIITTYQMLINNWQQLSSFRG-----------QEFVWDY 224
Cdd:cd18008   75 SQWKDEIEKhtKPGSLKVYVYHGSKRIKSIEELSDY----DIVITTYGTLASEFPKNKKGGGrdskekeasplHRIRWYR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  225 VILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFacqgsllGTLKTFkmeYENPITRAREKDATP 304
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRF-------LRVEPF---GDYPWFNSDISKPFS 220
                        250       260
                 ....*....|....*....|....
gi 58331268  305 GEKALGFkisENLMAIIKPYFLRR 328
Cdd:cd18008  221 KNDRKAL---ERLQALLKPILLRR 241
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
96-328 1.91e-43

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 157.90  E-value: 1.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMfdASLVN----HvLLIMPTNLINTWVKEFIKWTPGM 171
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNG-ILADEMGLGKTIQTIALLAHL--ACEKGnwgpH-LIVVPTSVMLNWEMEFKRWCPGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  172 RVKTFHGpSKDERTRnlnriqQRNG--------VIITTYQMLInnwQQLSSFRGQEfvWDYVILDEAHKIKTSSTKSAIC 243
Cdd:cd18003   77 KILTYYG-SAKERKL------KRQGwmkpnsfhVCITSYQLVV---QDHQVFKRKK--WKYLILDEAHNIKNFKSQRWQT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  244 ARAIPASNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENPITRAREkdatpGEKALGFKISENLMAIIKP 323
Cdd:cd18003  145 LLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMP-HIFQSHQEFKEWFSNPLTAMSE-----GSQEENEELVRRLHKVLRP 218

                 ....*
gi 58331268  324 YFLRR 328
Cdd:cd18003  219 FLLRR 223
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
96-273 4.55e-42

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 152.54  E-value: 4.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDgRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKT 175
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQK-KLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FHGpSKDERTRNLNRIQQRNG---VIITTYQMLINNWQQLSSFRGQEFvwDYVILDEAHKIKTSSTKSAICARAIPASNR 252
Cdd:cd17998   80 YYG-SQEERKHLRYDILKGLEdfdVIVTTYNLATSNPDDRSFFKRLKL--NYVVYDEGHMLKNMTSERYRHLMTINANFR 156
                        170       180
                 ....*....|....*....|.
gi 58331268  253 LLLTGTPIQNNLQELWSLFDF 273
Cdd:cd17998  157 LLLTGTPLQNNLLELMSLLNF 177
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
96-328 2.60e-41

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 151.63  E-value: 2.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRkGGILADDMGLGKTVQIIAFLSGMFDASLVNH-VLLIMPTNLINTWVKEFIKWTPgMRVK 174
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRR-NCILADEMGLGKTIQSIAFLEHLYQVEGIRGpFLVIAPLSTIPNWQREFETWTD-MNVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGPS-------------KDERTRNLNRIQQRNgVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSA 241
Cdd:cd17995   79 VYHGSGesrqiiqqyemyfKDAQGRKKKGVYKFD-VLITTYEMVIADAEELRKIP-----WRVVVVDEAHRLKNRNSKLL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSlLGTLKTFKMEYenpitrareKDATPGEKAlgfkisENLMAII 321
Cdd:cd17995  153 QGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEK-FPSSEEFLEEF---------GDLKTAEQV------EKLQALL 216

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd17995  217 KPYMLRR 223
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
95-330 5.99e-41

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 150.98  E-value: 5.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFLYSLYrDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNH-VLLIMPTNLINTWVKEFIKWTPGMRV 173
Cdd:cd17996    3 TLKEYQLKGLQWMVSLY-NNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGpYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  174 KTFHGPsKDERTRNLNriQQRNG---VIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTK-SAICARAIPA 249
Cdd:cd17996   82 IVYKGT-PDVRKKLQS--QIRAGkfnVLLTTYEYIIKDKPLLSKIK-----WKYMIIDEGHRMKNAQSKlTQTLNTYYHA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENP--ITRAREKDATPGEKALgfKISENLMAIIKPYFLR 327
Cdd:cd17996  154 RYRLLLTGTPLQNNLPELWALLNFLLP-KIFKSCKTFEQWFNTPfaNTGEQVKIELNEEETL--LIIRRLHKVLRPFLLR 230

                 ...
gi 58331268  328 RTK 330
Cdd:cd17996  231 RLK 233
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
99-328 3.96e-37

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 140.30  E-value: 3.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   99 HQKEGIAFLY----SLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDAS-----LVNHVLLIMPTNLINTWVKEFIKWTp 169
Cdd:cd18067    4 HQREGVKFLYrcvtGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSpqckpEIDKAIVVSPSSLVKNWANELGKWL- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  170 GMRVKTF--HGPSKDERTRNLNRIQQRNG------VIITTYQMLINNWQQLssfrgQEFVWDYVILDEAHKIKTSSTKSA 241
Cdd:cd18067   83 GGRLQPLaiDGGSKKEIDRKLVQWASQQGrrvstpVLIISYETFRLHVEVL-----QKGEVGLVICDEGHRLKNSDNQTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDATPGEKALGFKISENLMAII 321
Cdd:cd18067  158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPG-ILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIV 236

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd18067  237 NRCIIRR 243
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
96-328 4.19e-37

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 139.95  E-value: 4.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLsgmfdASLVNH------VLLIMPTNLINTWVKEFIKWTP 169
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQG-INGILADEMGLGKTVQSIAVL-----AHLAEEhniwgpFLVIAPASTLHNWQQEISRFVP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  170 GMRVKTFHGPSKDERT--RNLNRIQQ--RNG---VIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAI 242
Cdd:cd18002   75 QFKVLPYWGNPKDRKVlrKFWDRKNLytRDApfhVVITSYQLVVQDEKYFQRVK-----WQYMVLDEAQAIKSSSSSRWK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  243 CARAIPASNRLLLTGTPIQNNLQELWSLFDFaCQGSLLGTLKTFKMEYENPITRAREKDATPGEKALgfkisENLMAIIK 322
Cdd:cd18002  150 TLLSFHCRNRLLLTGTPIQNSMAELWALLHF-IMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQL-----KRLHMILK 223

                 ....*.
gi 58331268  323 PYFLRR 328
Cdd:cd18002  224 PFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
95-328 3.63e-34

DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350751 [Multi-domain]  Cd Length: 218  Bit Score: 130.94  E-value: 3.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFL-YSLYRDgrKGGILADDMGLGKTVQIIAFLSGMFDA-SLVNHVLLIMPTNLINTWVKEFIKWTPGMR 172
Cdd:cd17993    1 ELRDYQLTGLNWLaHSWCKG--NNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWAPDMN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  173 VKTFHGpskDERTRNLnrIQQ-----------RNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSA 241
Cdd:cd17993   79 VIVYLG---DIKSRDT--IREyefyfsqtkklKFNVLLTTYEIILKDKAFLGSIK-----WQYLAVDEAHRLKNDESLLY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSLlgtlkTFKMEYENPITRAREKDAtpgekalgfkisENLMAII 321
Cdd:cd17993  149 EALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKF-----DIWEEFEEEHDEEQEKGI------------ADLHKEL 211

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd17993  212 EPFILRR 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
95-335 1.59e-33

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 130.17  E-value: 1.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVN--HVLLImPTNLINTWVKEFIKWTPGMR 172
Cdd:cd18064   15 KLRDYQVRGLNWLISLYENG-INGILADEMGLGKTLQTISLLGYMKHYRNIPgpHMVLV-PKSTLHNWMAEFKRWVPTLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  173 VKTFHGpSKDERTRNLNRIQQRN--GVIITTYQMLInnwQQLSSFRgqEFVWDYVILDEAHKIKTSSTKSAICARAIPAS 250
Cdd:cd18064   93 AVCLIG-DKDQRAAFVRDVLLPGewDVCVTSYEMLI---KEKSVFK--KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  251 NRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENpitrarekDATPGEKalgfKISENLMAIIKPYFLRRTK 330
Cdd:cd18064  167 NRLLLTGTPLQNNLHELWALLNFLLP-DVFNSAEDFDSWFDT--------NNCLGDQ----KLVERLHMVLRPFLLRRIK 233

                 ....*
gi 58331268  331 EDVQK 335
Cdd:cd18064  234 ADVEK 238
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
99-309 6.76e-33

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 127.62  E-value: 6.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   99 HQKEGIAFLY-----SLYR---DGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKW--- 167
Cdd:cd18069    4 HQIGGIRFLYdniieSLERykgSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWlpp 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  168 ---TPGMRVKTFH-------GPSKDERTRNLNRIQQRNGVIITTYQMlinnwqqlssFRGQEFVwDYVILDEAHKIKTSS 237
Cdd:cd18069   84 peaLPNVRPRPFKvfilndeHKTTAARAKVIEDWVKDGGVLLMGYEM----------FRLRPGP-DVVICDEGHRIKNCH 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58331268  238 TKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDATPGEKAL 309
Cdd:cd18069  153 ASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPD-FLGTRQEFSNMFERPILNGQCVDSTPQDVKL 223
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
96-330 2.03e-32

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 126.29  E-value: 2.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMFDASLVN--HVLLImPTNLINTWVKEFIKWTPGMRV 173
Cdd:cd18065   16 LRDYQVRGLNWMISLYENG-VNGILADEMGLGKTLQTIALLGYLKHYRNIPgpHMVLV-PKSTLHNWMNEFKRWVPSLRA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  174 KTFHGpSKDERTRNLNRIQQRN--GVIITTYQMLInnwQQLSSFRgqEFVWDYVILDEAHKIKTSSTKSAICARAIPASN 251
Cdd:cd18065   94 VCLIG-DKDARAAFIRDVMMPGewDVCVTSYEMVI---KEKSVFK--KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  252 RLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENpitrarekdatpgEKALG-FKISENLMAIIKPYFLRRTK 330
Cdd:cd18065  168 RLLLTGTPLQNNLHELWALLNFLLP-DVFNSADDFDSWFDT-------------KNCLGdQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
92-330 2.08e-32

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 127.08  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   92 LHNQLFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNH-VLLIMPTNLINTWVKEFIKWTPG 170
Cdd:cd18062   20 VNGVLKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGpFLIIVPLSTLSNWVYEFDKWAPS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  171 MRVKTFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTK-SAICARAIPA 249
Cdd:cd18062   99 VVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIR-----WKYMIVDEGHRMKNHHCKlTQVLNTHYVA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENPITRAREK-DATPGEKALgfkISENLMAIIKPYFLRR 328
Cdd:cd18062  174 PRRLLLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKvDLNEEETIL---IIRRLHKVLRPFLLRR 249

                 ..
gi 58331268  329 TK 330
Cdd:cd18062  250 LK 251
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
99-304 6.00e-32

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 125.39  E-value: 6.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   99 HQKEGIAFLY-----SLYRDGRK---GGILADDMGLGKTVQIIAFLSGMF---DASLVNHVLLIMPTNLINTWVKEFIKW 167
Cdd:cd18068    4 HQVDGVQFMWdccceSLKKTKKSpgsGCILAHCMGLGKTLQVVTFLHTVLlceKLENFSRVLVVCPLNTVLNWLNEFEKW 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  168 TPGM------------RVKTfhgpsKDERTRNLNRIQQRNGVIITTYQM---LINNWQQLSSFRGQEFVW--------DY 224
Cdd:cd18068   84 QEGLkdeekievnelaTYKR-----PQERSYKLQRWQEEGGVMIIGYDMyriLAQERNVKSREKLKEIFNkalvdpgpDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  225 VILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDATP 304
Cdd:cd18068  159 VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPN-LLGTIKEFRNRFVNPIQNGQCADSTL 237
DEXDc smart00487
DEAD-like helicases superfamily;
88-273 1.08e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.08e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268      88 LYRELHNQLFEHQKEGIAFLYSLYRDGrkggILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPT-NLINTWVKEFIK 166
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDV----ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKK 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     167 WTPGMRVKT---FHGPSKDERTRNLNRiqQRNGVIITTYQMLINNWQQLSSFRGQefvWDYVILDEAHKIKTSSTKS--- 240
Cdd:smart00487   77 LGPSLGLKVvglYGGDSKREQLRKLES--GKTDILVTTPGRLLDLLENDKLSLSN---VDLVILDEAHRLLDGGFGDqle 151
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 58331268     241 AICARAIPASNRLLLTGTP---IQNNLQELWSLFDF 273
Cdd:smart00487  152 KLLKLLPKNVQLLLLSATPpeeIENLLELFLNDPVF 187
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
92-330 1.11e-30

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 122.09  E-value: 1.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   92 LHNQLFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNH-VLLIMPTNLINTWVKEFIKWTPG 170
Cdd:cd18063   20 INGTLKHYQLQGLEWMVSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRLNGpYLIIVPLSTLSNWTYEFDKWAPS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  171 MRVKTFHGPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTK-SAICARAIPA 249
Cdd:cd18063   99 VVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIR-----WKYMIVDEGHRMKNHHCKlTQVLNTHYVA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  250 SNRLLLTGTPIQNNLQELWSLFDFACQgSLLGTLKTFKMEYENPITRAREK-DATPGEKALgfkISENLMAIIKPYFLRR 328
Cdd:cd18063  174 PRRILLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGERvDLNEEETIL---IIRRLHKVLRPFLLRR 249

                 ..
gi 58331268  329 TK 330
Cdd:cd18063  250 LK 251
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
99-328 1.46e-30

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 120.62  E-value: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   99 HQKEGIAFLySLYRDGRKGGILADDMGLGKTVQIIAFLSGM-FDASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVKTFH 177
Cdd:cd18006    4 YQLEGVNWL-LQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVITYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  178 GpSKDERTRNLNRIQQRN--GVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASNRLLL 255
Cdd:cd18006   83 G-DKEKRLDLQQDIKSTNrfHVLLTTYEICLKDASFLKSFP-----WASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58331268  256 TGTPIQNNLQELWSLFDFaCQGSLLGtlktfKMEYENPITRAREKDATPGekalgfkISENLMAIIKPYFLRR 328
Cdd:cd18006  157 TGTPIQNSLQELYALLSF-IEPNVFP-----KDKLDDFIKAYSETDDESE-------TVEELHLLLQPFLLRR 216
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
96-328 8.94e-30

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 119.12  E-value: 8.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLysLYRDGRK--GGILADDMGLGKTVQIIAFL-----------------SGMFDASLVNHV------LL 150
Cdd:cd18072    1 LLLHQKQALAWL--LWRERQKprGGILADDMGLGKTLTMIALIlaqkntqnrkeeekekaLTEWESKKDSTLvpsagtLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  151 IMPTNLINTWVKEFIKWTPG--MRVKTFHGPSKDERTRNLNRIQqrngVIITTYQMLINNWQQLSSFRGQEFV----WDY 224
Cdd:cd18072   79 VCPASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEVLRDYD----IVITTYSLVAKEIPTYKEESRSSPLfriaWAR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  225 VILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDFA-CqgSLLGTLKTFKMEYENpitrarekdat 303
Cdd:cd18072  155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLrC--SPFDDLKVWKKQVDN----------- 221
                        250       260
                 ....*....|....*....|....*
gi 58331268  304 pgEKALGfkiSENLMAIIKPYFLRR 328
Cdd:cd18072  222 --KSRKG---GERLNILTKSLLLRR 241
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
95-328 1.94e-29

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 117.80  E-value: 1.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFL-YSLYRDGRKggILADDMGLGKTVQIIAFLSGMFDA-SLVNHVLLIMPTNLINTWVKEFIKWTPGMR 172
Cdd:cd18054   20 ELRDYQLEGLNWLaHSWCKNNSV--ILADEMGLGKTIQTISFLSYLFHQhQLYGPFLLVVPLSTLTSWQREFEIWAPEIN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  173 VKTFHGPSKDERT-RNLNRIQQRN-----GVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSST---KSAIC 243
Cdd:cd18054   98 VVVYIGDLMSRNTiREYEWIHSQTkrlkfNALITTYEILLKDKTVLGSIN-----WAFLGVDEAHRLKNDDSllyKTLID 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  244 ARAipaSNRLLLTGTPIQNNLQELWSLFDFacqgsLLGTLKTFKMEYENPITRAREKdatpgekalGFkisENLMAIIKP 323
Cdd:cd18054  173 FKS---NHRLLITGTPLQNSLKELWSLLHF-----IMPEKFEFWEDFEEDHGKGREN---------GY---QSLHKVLEP 232

                 ....*
gi 58331268  324 YFLRR 328
Cdd:cd18054  233 FLLRR 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
96-328 2.15e-28

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 114.37  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFL-YSLYRdgRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPgMRVK 174
Cdd:cd18058    1 LREYQLEGMNWLlFNWYN--RKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGPS-------------KDERTRNLNRIQQRNGViITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSA 241
Cdd:cd18058   78 VYHGSQisrqmiqqyemyyRDEQGNPLSGIFKFQVV-ITTFEMILADCPELKKIN-----WSCVIIDEAHRLKNRNCKLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFaCQGSLLGTLKTFKMEYENPITRAREKdatpgekalgfkiseNLMAII 321
Cdd:cd18058  152 EGLKLMALEHKVLLTGTPLQNSVEELFSLLNF-LEPSQFPSETTFLEEFGDLKTEEQVK---------------KLQSIL 215

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd18058  216 KPMMLRR 222
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
96-273 6.61e-27

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 110.64  E-value: 6.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSL--------YRDGRK--------------------GGILADDMGLGKTVQIIAFLsgmfdasLVNH 147
Cdd:cd18071    1 LLPHQKQALAWMVSRensqdlppFWEEAVglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI-------LANF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  148 VLLIMPTNLINTWVKEFIKWT-PG-MRVKTFHGPskdERTRNLNRIQQRNgVIITTYQMLINNWQQLSSFRGQEFVWDYV 225
Cdd:cd18071   74 TLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGG---ERNRDPKLLSKYD-IVLTTYNTLASDFGAKGDSPLHTINWLRV 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 58331268  226 ILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18071  150 VLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
96-328 1.09e-26

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 109.37  E-value: 1.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFL-YSLYrdGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPgMRVK 174
Cdd:cd18060    1 LREYQLEGVNWLlFNWY--NRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGP-------------SKDERTRNLNRIQQRNGvIITTYQMLINNWQQLssfrgQEFVWDYVILDEAHKIKTSSTKSA 241
Cdd:cd18060   78 VYHGSlasrqmiqqyemyCKDSRGRLIPGAYKFDA-LITTFEMILSDCPEL-----REIEWRCVIIDEAHRLKNRNCKLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFacqgsllgtlkTFKMEYENPITRAREKDATPGEKALgfkisENLMAII 321
Cdd:cd18060  152 DSLKHMDLEHKVLLTGTPLQNTVEELFSLLHF-----------LEPSQFPSESEFLKDFGDLKTEEQV-----QKLQAIL 215

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd18060  216 KPMMLRR 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
460-574 1.35e-25

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    460 GKMIFLMDLLKRLRdeGHQTLVFSQSRQILNIiERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKdySVFLLTTQVG 539
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQE-EREEILEDFRKGK--IDVLVATDVA 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 58331268    540 GVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIG 574
Cdd:pfam00271   75 ERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
96-292 1.70e-24

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 102.13  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNHVLLI-MPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVsAPLSTIINWEREFEMWAPDFYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGpskdertrnlnriqqrNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSAICARAIPASNRLL 254
Cdd:cd17994   80 TYVG----------------DHVLLTSYELISIDQAILGSID-----WAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 58331268  255 LTGTPIQNNLQELWSLFDFACQGSlLGTLKTFKMEYEN 292
Cdd:cd17994  139 LTGTPLQNNLEELFHLLNFLTPER-FNNLQGFLEEFAD 175
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
96-328 2.16e-24

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 102.80  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTPgMRVKT 175
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNC-ILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FHGPSKDERTRNLNRIQQRNG------------VIITTYQMLINNWQQLssfrgQEFVWDYVILDEAHKIKTSSTKSAIC 243
Cdd:cd18059   79 YHGSQASRRTIQLYEMYFKDPqgrvikgsykfhAIITTFEMILTDCPEL-----RNIPWRCVVIDEAHRLKNRNCKLLEG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  244 ARAIPASNRLLLTGTPIQNNLQELWSLFDFACQGSlLGTLKTFKMEYENPITRARekdatpgekalgfkiSENLMAIIKP 323
Cdd:cd18059  154 LKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSR-FPSETTFMQEFGDLKTEEQ---------------VQKLQAILKP 217

                 ....*
gi 58331268  324 YFLRR 328
Cdd:cd18059  218 MMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
95-273 1.04e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 101.28  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFLYSLYRDGrKGGILADDMGLGKTVQIIAFLSGMF-DASLVNHVLLIMPTNLINTWVKEFIKWTPGMRV 173
Cdd:cd18053   20 ELRDYQLNGLNWLAHSWCKG-NSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  174 KTFHGpskDERTRNLNRIQQ---------RNGVIITTYQMLINNwqqlSSFRGQeFVWDYVILDEAHKIKTSSTKSAICA 244
Cdd:cd18053   99 VVYLG---DINSRNMIRTHEwmhpqtkrlKFNILLTTYEILLKD----KSFLGG-LNWAFIGVDEAHRLKNDDSLLYKTL 170
                        170       180
                 ....*....|....*....|....*....
gi 58331268  245 RAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18053  171 IDFKSNHRLLITGTPLQNSLKELWSLLHF 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
96-303 1.09e-23

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 100.36  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFlySLYRDGRkgGILADDMGLGKTVQIIAFlsgmfdASLVNH---VLLIMPTNLINTWVKEFIKWTPGMr 172
Cdd:cd18010    1 LLPFQREGVCF--ALRRGGR--VLIADEMGLGKTVQAIAI------AAYYREewpLLIVCPSSLRLTWADEIERWLPSL- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  173 vktfhgPSKDERTRNLNRIQQRNG---VIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTK-SAICARAIP 248
Cdd:cd18010   70 ------PPDDIQVIVKSKDGLRDGdakVVIVSYDLLRRLEKQLLARK-----FKVVICDESHYLKNSKAKrTKAALPLLK 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 58331268  249 ASNR-LLLTGTPIQNNLQELWSLFDFACQGsLLGTLKTFKMEYENPITRAREKDAT 303
Cdd:cd18010  139 RAKRvILLSGTPALSRPIELFTQLDALDPK-LFGRFHDFGRRYCAAKQGGFGWDYS 193
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
96-328 3.83e-23

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 99.31  E-value: 3.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFL-YSLYRdgRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEFIKWTpGMRVK 174
Cdd:cd18061    1 LREYQLEGLNWLlFNWYN--RRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGP-------------SKDERTRNLnRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKIKTSSTKSA 241
Cdd:cd18061   78 VYHGSlisrqmiqqyemyFRDSQGRII-RGAYRFQAIITTFEMILGGCPELNAID-----WRCVIIDEAHRLKNKNCKLL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  242 ICARAIPASNRLLLTGTPIQNNLQELWSLFDFaCQGSLLGTLKTFKMEYENPITRARekdatpgekalgfkiSENLMAII 321
Cdd:cd18061  152 EGLKLMNLEHKVLLTGTPLQNTVEELFSLLHF-LEPLRFPSESTFMQEFGDLKTEEQ---------------VQKLQAIL 215

                 ....*..
gi 58331268  322 KPYFLRR 328
Cdd:cd18061  216 KPMMLRR 222
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
96-296 6.06e-21

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 92.80  E-value: 6.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLyslyRDGRKGGILADdMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLI-NTWVKEFIKWT--PGMR 172
Cdd:cd18013    1 PHPYQKVAINFI----IEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVArSTWPDEVEKWNhlRNLT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  173 VKTFHGpSKDERTRNLNriQQRNGVIITtyqmlINNWQQLSSFRGQEFVWDYVILDEAHKIKTSSTKSAICARAI-PASN 251
Cdd:cd18013   76 VSVAVG-TERQRSKAAN--TPADLYVIN-----RENLKWLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVrPVIK 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 58331268  252 RLL-LTGTPIQNNLQELWSLFDFACQGSLLG-TLKTFKMEYENPITR 296
Cdd:cd18013  148 RLIgLTGTPSPNGLMDLWAQIALLDQGERLGrSITAYRERWFDPDKR 194
HELICc smart00490
helicase superfamily c-terminal domain;
491-574 6.27e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 6.27e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268     491 IIERLLKNRHFKTLRIDGTVTHLlEREKRINLFQQNKdySVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRV 570
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQE-EREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 58331268     571 YRIG 574
Cdd:smart00490   79 GRAG 82
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
96-273 1.93e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 88.91  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNHVLLI-MPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVsAPLSTIINWEREFQMWAPDFYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGpSKDERT---------------------RNLNRIQQRNGVIITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKI 233
Cdd:cd18055   80 TYTG-DKDSRAiirenefsfddnavkggkkafKMKREAQVKFHVLLTSYELVTIDQAALGSIR-----WACLVVDEAHRL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 58331268  234 KTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18055  154 KNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNF 193
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
96-273 3.10e-19

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 88.20  E-value: 3.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMFDASLVNHVLLI-MPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVsAPLSTIINWEREFEMWAPDMYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGpSKDERT-----------------RNLNRIQQRNGV----IITTYQMLINNWQQLSSFRgqefvWDYVILDEAHKI 233
Cdd:cd18056   80 TYVG-DKDSRAiirenefsfednairggKKASRMKKEASVkfhvLLTSYELITIDMAILGSID-----WACLIVDEAHRL 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 58331268  234 KTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18056  154 KNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNF 193
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
96-273 1.16e-18

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 86.66  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRKGgILADDMGLGKTVQIIAFLSGMF-DASLVNHVLLIMPTNLINTWVKEFIKWTPGMRVK 174
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDT-ILADEMGLGKTVQTIVFLYSLYkEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  175 TFHGpskDERTRNLNRIQQ--------RNG---------------VIITTYQMLINNWQQLSSFRgqefvWDYVILDEAH 231
Cdd:cd18057   80 TYTG---DKESRSVIRENEfsfednaiRSGkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIE-----WACLVVDEAH 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 58331268  232 KIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18057  152 RLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNF 193
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
96-273 8.87e-18

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 84.70  E-value: 8.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLyrdgrkGGILADDMGLGKTVQIIAFL-----------SGMFDASLV---NHV------------L 149
Cdd:cd18070    1 LLPYQRRAVNWMLVP------GGILADEMGLGKTVEVLALIllhprpdndldAADDDSDEMvccPDClvaetpvsskatL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  150 LIMPTNLINTWVKEFIKWTPG-MRVKTFHGPSKD--ERTRNLNRIQQRNgVIITTYQML---INNWQQLSSFRG-QEFV- 221
Cdd:cd18070   75 IVCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDgaLASPAPEILAEYD-IVVTTYDVLrteLHYAEANRSNRRrRRQKr 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58331268  222 ------------WDYVILDEAHKIKTSSTKSAICARAIPASNRLLLTGTPIQNNLQELWSLFDF 273
Cdd:cd18070  154 yeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSF 217
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
96-270 2.84e-17

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 81.95  E-value: 2.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQkegIAFLYSLYRDGRKGGILADDMGLGKTVQIIAFLSGMFDASLVNHVLLIMPTNLINTWVKEfikwtpgMRVKt 175
Cdd:cd18011    1 PLPHQ---IDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDE-------LQDK- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  176 FH-------GPSKDERTRNLNRIQQRNGVIITTYQMLINNWQQLSSFrgQEFVWDYVILDEAHKI-----KTSSTKSAIC 243
Cdd:cd18011   70 FGlpflildRETAAQLRRLIGNPFEEFPIVIVSLDLLKRSEERRGLL--LSEEWDLVVVDEAHKLrnsggGKETKRYKLG 147
                        170       180
                 ....*....|....*....|....*...
gi 58331268  244 ARAIPAS-NRLLLTGTPIQNNLQELWSL 270
Cdd:cd18011  148 RLLAKRArHVLLLTATPHNGKEEDFRAL 175
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
95-725 1.95e-16

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 84.31  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   95 QLFEHQKEGIAFLYSLYRDGRKGGILADDMGLGKTVqIIAFLsgMFDASLVNHVLLIMPT-NLINTWVKEFIKWTPGmrv 173
Cdd:COG1061   80 ELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTV-LALAL--AAELLRGKRVLVLVPRrELLEQWAEELRRFLGD--- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  174 KTFHGPSKDERTRnlnriqqrngVIITTYQMLINNwQQLSSFRGQefvWDYVILDEAHKIKTSSTKSAIcaRAIPASNRL 253
Cdd:COG1061  154 PLAGGGKKDSDAP----------ITVATYQSLARR-AHLDELGDR---FGLVIIDEAHHAGAPSYRRIL--EAFPAAYRL 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  254 LLTGTPI-QNNLQELWSLFDfacqgsllgtlktfKMEYENPITRAREKDatpgekalgfkisenlmaIIKPYflrrtked 332
Cdd:COG1061  218 GLTATPFrSDGREILLFLFD--------------GIVYEYSLKEAIEDG------------------YLAPP-------- 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  333 vqkkkssnpearlneknpdvdaicempslsrkndlIIWIRLVPLQEEIYRKFVSLDHIKELLMetrsplaelgvlkklcd 412
Cdd:COG1061  258 -----------------------------------EYYGIRVDLTDERAEYDALSERLREALA----------------- 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  413 hprllsaraccllnlgtfsaqdgnegEDSPDVDHIdqvtddtlmeesgkmifLMDLLKRLRDeGHQTLVFSQSRQILNII 492
Cdd:COG1061  286 --------------------------ADAERKDKI-----------------LRELLREHPD-DRKTLVFCSSVDHAEAL 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  493 ERLLKNRHFKTLRIDGTvTHLLEREKRINLFQQNKDysVFLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYR 572
Cdd:COG1061  322 AELLNEAGIRAAVVTGD-TPKKEREEILEAFRDGEL--RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLR 398
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  573 IGQ-KENVVVYRLITCGT-VEEKIYRRQVFKDSLIRQTTGEKKNPFRYFSKQELRELFTIEDLQNSVTQLQLQSLHA--- 647
Cdd:COG1061  399 PAPgKEDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDAlll 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  648 --AQRKSDIKLDEHIAYLQSLGIAGISDHDLMYTCDLSVKEELDVVEESHYIQQRVQKAQFLVEFESQNKEFLMEQQRTR 725
Cdd:COG1061  479 vlAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALLRLEELAALLLKE 558
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
96-259 2.16e-11

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 63.09  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLYSLYRDGRkgGILADDMGLGKTV---QIIAFLSgmfdaslVNHVLLIMPTN-LINTWVKEFIKWTPGM 171
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR--GILVLPTGSGKTLtalALIAYLK-------ELRTLIVVPTDaLLDQWKERFEDFLGDS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  172 RVKTFHGPSKDERTRNLnriqqrngVIITTYQMLINNwQQLSSFRGQEFvwDYVILDEAHKIkTSSTKSAICARAIpASN 251
Cdd:cd17926   72 SIGLIGGGKKKDFDDAN--------VVVATYQSLSNL-AEEEKDLFDQF--GLLIVDEAHHL-PAKTFSEILKELN-AKY 138

                 ....*...
gi 58331268  252 RLLLTGTP 259
Cdd:cd17926  139 RLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
116-258 4.28e-09

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 56.26  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  116 KGGILADDMGLGKTvqIIAFLSgMFDASLVNH--VLLIMPTN-LINTWVKEFIKW-TPGMRVKTFHGPSKDERtrNLNRI 191
Cdd:cd00046    2 ENVLITAPTGSGKT--LAALLA-ALLLLLKKGkkVLVLVPTKaLALQTAERLRELfGPGIRVAVLVGGSSAEE--REKNK 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58331268  192 QQRNGVIITTYQMLINNWQQLSSFRGQEFvwDYVILDEAHKIK-----TSSTKSAICARAIPASNRLLLTGT 258
Cdd:cd00046   77 LGDADIIIATPDMLLNLLLREDRLFLKDL--KLIIVDEAHALLidsrgALILDLAVRKAGLKNAQVILLSAT 146
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
107-258 1.18e-08

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 55.77  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  107 LYSLYRDGRKG-GILADDMGLGKTvqiiafLSGMFDASLVNHVLLIMPTNLINT--WVKEFIKWT--PGMRVKTFHGPSK 181
Cdd:cd18029   17 LSKMFGNGRARsGVIVLPCGAGKT------LVGITAACTIKKSTLVLCTSAVSVeqWRRQFLDWTtiDDEQIGRFTSDKK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  182 DertrnlnrIQQRNGVIITTYQMLIN------NWQQLSSF-RGQEfvWDYVILDEAHKI------KTSSTKSAICaraip 248
Cdd:cd18029   91 E--------IFPEAGVTVSTYSMLANtrkrspESEKFMEFiTERE--WGLIILDEVHVVpapmfrRVLTLQKAHC----- 155
                        170
                 ....*....|
gi 58331268  249 asnRLLLTGT 258
Cdd:cd18029  156 ---KLGLTAT 162
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
532-582 2.13e-08

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 52.32  E-value: 2.13e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 58331268  532 FLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKENVVVY 582
Cdd:cd18785   25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
455-632 3.21e-07

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 54.74  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  455 LMEESG----KMIFLMDLLKRLRDE--GHQTLVFSQSRQILNIIERLLKNRHFKTLRI-----DGTVTHLL--EREKRIN 521
Cdd:COG1111  326 LAEEADiehpKLSKLREILKEQLGTnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqasKEGDKGLTqkEQIEILE 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  522 LFQQNkDYSVfLLTTQVGGVGLTLTAATRVVIFDPSWNPATDAQAVDRVYRIGQKEnVVVyrLITCGTVEEKIY-----R 596
Cdd:COG1111  406 RFRAG-EFNV-LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR-VVV--LIAKGTRDEAYYwssrrK 480
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 58331268  597 RQVFKDSLIRQTTGEKKNPFRYFSKQELRELFTIED 632
Cdd:COG1111  481 EKKMKSILKKLKKLLDKQEKEKLKESAQATLDEFES 516
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
125-262 1.18e-06

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 49.93  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    125 GLGKTvqiIAFLSGMFDASLVNH----VLLIMPT-NLINTWVKEFIKWTPGMRVK---TFHGPSKDERTRNLNRIQqrng 196
Cdd:pfam00270   24 GSGKT---LAFLLPALEALDKLDngpqALVLAPTrELAEQIYEELKKLGKGLGLKvasLLGGDSRKEQLEKLKGPD---- 96
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58331268    197 VIITTYQMLINNWQQLSSFRGQEfvwdYVILDEAHKIKTSSTKSAI--CARAIPASNR-LLLTGTPIQN 262
Cdd:pfam00270   97 ILVGTPGRLLDLLQERKLLKNLK----LLVLDEAHRLLDMGFGPDLeeILRRLPKKRQiLLLSATLPRN 161
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
96-231 5.16e-05

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 45.27  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268   96 LFEHQKEGIAFLyslyRDGRKGgILADDMGLGKTvqiIAFLSGMFDASLVNH---VLLIMPTN-LINTWVKEFIKWTPGM 171
Cdd:cd17923    1 LYSHQAEAIEAA----RAGRSV-VVTTGTASGKS---LCYQLPILEALLRDPgsrALYLYPTKaLAQDQLRSLRELLEQL 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268  172 ----RVKTFHGPSKDERTRnlnRIQQRNGVIITT------YQMLINNWQQLSSFRGqefvWDYVILDEAH 231
Cdd:cd17923   73 glgiRVATYDGDTPREERR---AIIRNPPRILLTnpdmlhYALLPHHDRWARFLRN----LRYVVLDEAH 135
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
455-591 2.56e-03

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 41.16  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58331268    455 LMEESGKMIFLMDLLK----RLRDEGHQTLVFSQSRQILNIIERLLKNRHFKTLRIDGTvthLLEREKR-INLFQQNKDY 529
Cdd:pfam11496   85 LAYTSGKFLVLNDLVNllieRDRKEPINVAIVARSGKTLDLVEALLLGKGLSYKRYSGE---MLYGENKkVSDSGNKKIH 161
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 58331268    530 SV---FLLTTQVGGVGLTLTAATR---VVIFDPSWNPATDAQAVDRVYRIGQKENVVVYRLITCGTVE 591
Cdd:pfam11496  162 STtchLLSSTGQLTNDDSLLENYKfdlIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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